Analytical Data
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基因名
SLC23A1
- Application
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别名
hSVCT1; Na(+)/L-ascorbic acid transporter 1; S23A1_HUMAN; Slc23a1; Sodium-dependent vitamin C transporter 1; solute carrier family 23 (nucleobase transporters); member 1; Solute carrier family 23 member 1; SVCT1; Yolk sac permease-like molecule 3; YSPL3
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9UHI7
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表达区间
1-259 aa
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氨基酸序列
MRAQEDLEGRTQHETTRDPSTPLPTEPKFDMLYKIEDVPPWYLCILLGFQHYLTCFSGTIAVPFLLAEALCVGHDQHMVSQLIGTIFTCVGMFCTLFGMITAVGLSNLQFVDMNSSRNLFALGFSMFFGLTLPNYLESNPGAINTGILEVDQILIVLLTTEMFVGGCLAFILDNTVPGSPEERGLIQWKAGAHANSDMSSSLKSYDFPIGMGIVKRITFLRYIPICPVFKGFSSSSKDQIAIPEDTPENTETASVCTKV
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分子量
54.23 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
SLC23A1, a member of the solute carrier family, functions as a sodium-dependent phosphate transporter and plays a crucial role in the regulation of vitamin C homeostasis in humans. The protein is primarily responsible for the uptake of ascorbic acid in various tissues, contributing to antioxidant defense and collagen synthesis. Dysfunction of SLC23A1 has been implicated in various pathologies, including scurvy, metabolic disorders, and certain types of cancer. Recent studies have highlighted the importance of SLC23A1 not only in dietary vitamin C absorption but also in mediating its physiological effects. The generation of recombinant SLC23A1 protein has become a significant focus of research, as it allows for in-depth characterization of the transport mechanisms and substrate specificity of this protein. By producing and studying recombinant SLC23A1, researchers aim to elucidate its structure-function relationships and how mutations or alterations in its expression can lead to disease. Furthermore, understanding the dynamics of SLC23A1 may provide insights into potential therapeutic targets for diseases related to vitamin C transport and homeostasis. Ultimately, the exploration of SLC23A1 at the molecular level holds promise for advancing knowledge in nutrient transport, metabolism, and related health implications.
